CC14A_HUMAN
ID CC14A_HUMAN Reviewed; 594 AA.
AC Q9UNH5; A6MA65; B1AQ14; B1AQ15; O43171; O60727; O60728; Q52LH9; Q8IXX0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Dual specificity protein phosphatase CDC14A;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=CDC14 cell division cycle 14 homolog A;
GN Name=CDC14A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9367992; DOI=10.1074/jbc.272.47.29403;
RA Li L., Ernsting B.R., Wishart M.J., Lohse D.L., Dixon J.E.;
RT "A family of putative tumor suppressors is structurally and functionally
RT conserved in humans and yeast.";
RL J. Biol. Chem. 272:29403-29406(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10409437; DOI=10.1006/geno.1999.5863;
RA Wong A.K.C., Chen Y., Lian L., Ha P.C., Petersen K., Laity K., Carillo A.,
RA Emerson M., Heichman K., Gupte J., Tavtigian S.V., Teng D.H.-F.;
RT "Genomic structure, chromosomal location, and mutation analysis of the
RT human CDC14A gene.";
RL Genomics 59:248-251(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta;
RA Hao L., Baskerville C., Charbonneau H.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Belyaev A.S., Kolokithas A., Monell C.R.;
RT "Human CDC14A splice variant.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-345 AND PHE-589.
RG NIEHS SNPs program;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP DEPHOSPHORYLATION OF FZR1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-278.
RX PubMed=11598127; DOI=10.1074/jbc.m108126200;
RA Bembenek J., Yu H.;
RT "Regulation of the anaphase-promoting complex by the dual specificity
RT phosphatase human Cdc14a.";
RL J. Biol. Chem. 276:48237-48242(2001).
RN [10]
RP SUBSTRATE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-251; CYS-278 AND ARG-284.
RX PubMed=12134069; DOI=10.1091/mbc.01-11-0535;
RA Kaiser B.K., Zimmerman Z.A., Charbonneau H., Jackson P.K.;
RT "Disruption of centrosome structure, chromosome segregation, and
RT cytokinesis by misexpression of human Cdc14A phosphatase.";
RL Mol. Biol. Cell 13:2289-2300(2002).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF MET-362 AND ILE-364.
RX PubMed=11901424; DOI=10.1038/ncb777;
RA Mailand N., Lukas C., Kaiser B.K., Jackson P.K., Bartek J., Lukas J.;
RT "Deregulated human Cdc14A phosphatase disrupts centrosome separation and
RT chromosome segregation.";
RL Nat. Cell Biol. 4:317-322(2002).
RN [12]
RP INTERACTION WITH KIF20A, AND SUBCELLULAR LOCATION.
RX PubMed=15263015; DOI=10.1083/jcb.200403084;
RA Gruneberg U., Neef R., Honda R., Nigg E.A., Barr F.A.;
RT "Relocation of Aurora B from centromeres to the central spindle at the
RT metaphase to anaphase transition requires MKlp2.";
RL J. Cell Biol. 166:167-172(2004).
RN [13]
RP FUNCTION AS SIRT2 PHOSPHATASE.
RX PubMed=17488717; DOI=10.1074/jbc.m702990200;
RA North B.J., Verdin E.;
RT "Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent
RT phosphorylation.";
RL J. Biol. Chem. 282:19546-19555(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND SER-583, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP INVOLVEMENT IN DFNB32, AND VARIANTS DFNB32 339-ARG--TYR-594 DEL AND
RP 376-ARG--TYR-594 DEL.
RX PubMed=27259055; DOI=10.1016/j.ajhg.2016.04.015;
RA Delmaghani S., Aghaie A., Bouyacoub Y., El Hachmi H., Bonnet C., Riahi Z.,
RA Chardenoux S., Perfettini I., Hardelin J.P., Houmeida A., Herbomel P.,
RA Petit C.;
RT "Mutations in CDC14A, encoding a protein phosphatase involved in hair cell
RT ciliogenesis, cause autosomal-recessive severe to profound deafness.";
RL Am. J. Hum. Genet. 98:1266-1270(2016).
RN [16]
RP FUNCTION, VARIANTS DFNB32 139-TYR--TYR-594 DEL; GLN-312; GLY-312; PRO-320;
RP 345-ARG--TYR-594 DEL AND 376-ARG--TYR-594 DEL, AND INVOLVEMENT IN DFNB32.
RX PubMed=29293958; DOI=10.1093/hmg/ddx440;
RA Imtiaz A., Belyantseva I.A., Beirl A.J., Fenollar-Ferrer C., Bashir R.,
RA Bukhari I., Bouzid A., Shaukat U., Azaiez H., Booth K.T., Kahrizi K.,
RA Najmabadi H., Maqsood A., Wilson E.A., Fitzgerald T.S., Tlili A.,
RA Olszewski R., Lund M., Chaudhry T., Rehman A.U., Starost M.F., Waryah A.M.,
RA Hoa M., Dong L., Morell R.J., Smith R.J.H., Riazuddin S., Masmoudi S.,
RA Kindt K.S., Naz S., Friedman T.B.;
RT "CDC14A phosphatase is essential for hearing and male fertility in mouse
RT and human.";
RL Hum. Mol. Genet. 27:780-798(2018).
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] TYR-493.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Dual-specificity phosphatase. Required for centrosome
CC separation and productive cytokinesis during cell division.
CC Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the
CC APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation
CC of mitotic cyclins and subsequent exit from mitosis. Required for
CC normal hearing (PubMed:29293958). {ECO:0000269|PubMed:11901424,
CC ECO:0000269|PubMed:12134069, ECO:0000269|PubMed:17488717,
CC ECO:0000269|PubMed:29293958, ECO:0000269|PubMed:9367992}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Interacts with KIF20A, which is required to localize CDC14 to
CC the midzone of the mitotic spindle. {ECO:0000269|PubMed:15263015}.
CC -!- INTERACTION:
CC Q9UNH5; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-7851002, EBI-1166928;
CC Q9UNH5; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-7851002, EBI-725606;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9367992}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:11901424, ECO:0000269|PubMed:12134069}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:11901424,
CC ECO:0000269|PubMed:15263015}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:15263015}. Cell projection, kinocilium
CC {ECO:0000250|UniProtKB:Q6GQT0}. Cell projection, stereocilium
CC {ECO:0000250|UniProtKB:Q6GQT0}. Note=Centrosomal during interphase,
CC released into the cytoplasm at the onset of mitosis. Subsequently
CC localizes to the mitotic spindle pole and at the central spindle
CC (PubMed:12134069, PubMed:11901424, PubMed:15263015). Present along both
CC the transient kinocilia of developing cochlear hair cells and the
CC persistent kinocilia of vestibular hair cells (By similarity).
CC {ECO:0000250|UniProtKB:Q6GQT0, ECO:0000269|PubMed:11901424,
CC ECO:0000269|PubMed:12134069, ECO:0000269|PubMed:15263015}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=CDC14A1;
CC IsoId=Q9UNH5-1; Sequence=Displayed;
CC Name=2; Synonyms=CDC14A2;
CC IsoId=Q9UNH5-2; Sequence=VSP_012037;
CC Name=3; Synonyms=CDC14A3;
CC IsoId=Q9UNH5-3; Sequence=VSP_012035, VSP_012036;
CC Name=4; Synonyms=CDC14A4;
CC IsoId=Q9UNH5-4; Sequence=VSP_012322, VSP_012323;
CC Name=5;
CC IsoId=Q9UNH5-5; Sequence=VSP_047597;
CC -!- DOMAIN: Composed of two structurally equivalent A and B domains that
CC adopt a dual specificity protein phosphatase (DSP) fold. {ECO:0000250}.
CC -!- DISEASE: Deafness, autosomal recessive, 32, with or without immotile
CC sperm (DFNB32) [MIM:608653]: A form of non-syndromic sensorineural
CC hearing loss. Sensorineural deafness results from damage to the neural
CC receptors of the inner ear, the nerve pathways to the brain, or the
CC area of the brain that receives sound information. DFNB32 is
CC characterized by prelingual, progressive, moderate to profound
CC sensorineural deafness. Some affected men are infertile.
CC {ECO:0000269|PubMed:27259055, ECO:0000269|PubMed:29293958}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88277.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc14a/";
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DR EMBL; AF000367; AAB88277.1; ALT_FRAME; mRNA.
DR EMBL; AF122013; AAD49217.1; -; mRNA.
DR EMBL; AF064102; AAC16659.1; -; mRNA.
DR EMBL; AF064103; AAC16660.1; -; mRNA.
DR EMBL; DQ530256; ABF74568.1; -; mRNA.
DR EMBL; AY623111; AAT38107.1; -; Genomic_DNA.
DR EMBL; AC104457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW72956.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72958.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72959.1; -; Genomic_DNA.
DR EMBL; BC038979; AAH38979.1; -; mRNA.
DR EMBL; BC093916; AAH93916.1; -; mRNA.
DR EMBL; BC093918; AAH93918.1; -; mRNA.
DR CCDS; CCDS769.1; -. [Q9UNH5-1]
DR CCDS; CCDS770.1; -. [Q9UNH5-2]
DR CCDS; CCDS771.1; -. [Q9UNH5-3]
DR CCDS; CCDS86000.1; -. [Q9UNH5-5]
DR RefSeq; NP_001306139.1; NM_001319210.1. [Q9UNH5-5]
DR RefSeq; NP_001306140.1; NM_001319211.1.
DR RefSeq; NP_001306141.1; NM_001319212.1.
DR RefSeq; NP_003663.2; NM_003672.3. [Q9UNH5-1]
DR RefSeq; NP_201569.1; NM_033312.2. [Q9UNH5-2]
DR RefSeq; NP_201570.1; NM_033313.2. [Q9UNH5-3]
DR AlphaFoldDB; Q9UNH5; -.
DR SMR; Q9UNH5; -.
DR BioGRID; 114126; 104.
DR IntAct; Q9UNH5; 45.
DR MINT; Q9UNH5; -.
DR STRING; 9606.ENSP00000354916; -.
DR BindingDB; Q9UNH5; -.
DR ChEMBL; CHEMBL1772926; -.
DR DEPOD; CDC14A; -.
DR iPTMnet; Q9UNH5; -.
DR PhosphoSitePlus; Q9UNH5; -.
DR BioMuta; CDC14A; -.
DR DMDM; 55976620; -.
DR EPD; Q9UNH5; -.
DR jPOST; Q9UNH5; -.
DR MassIVE; Q9UNH5; -.
DR PaxDb; Q9UNH5; -.
DR PeptideAtlas; Q9UNH5; -.
DR PRIDE; Q9UNH5; -.
DR ProteomicsDB; 792; -.
DR ProteomicsDB; 85289; -. [Q9UNH5-1]
DR ProteomicsDB; 85290; -. [Q9UNH5-2]
DR ProteomicsDB; 85291; -. [Q9UNH5-3]
DR ProteomicsDB; 85292; -. [Q9UNH5-4]
DR Antibodypedia; 19991; 322 antibodies from 32 providers.
DR DNASU; 8556; -.
DR Ensembl; ENST00000336454.5; ENSP00000336739.3; ENSG00000079335.20. [Q9UNH5-1]
DR Ensembl; ENST00000361544.11; ENSP00000354916.6; ENSG00000079335.20. [Q9UNH5-2]
DR Ensembl; ENST00000370124.8; ENSP00000359142.3; ENSG00000079335.20. [Q9UNH5-3]
DR Ensembl; ENST00000644813.1; ENSP00000496374.1; ENSG00000079335.20. [Q9UNH5-5]
DR GeneID; 8556; -.
DR KEGG; hsa:8556; -.
DR MANE-Select; ENST00000336454.5; ENSP00000336739.3; NM_003672.4; NP_003663.2.
DR UCSC; uc001dte.5; human. [Q9UNH5-1]
DR CTD; 8556; -.
DR DisGeNET; 8556; -.
DR GeneCards; CDC14A; -.
DR HGNC; HGNC:1718; CDC14A.
DR HPA; ENSG00000079335; Tissue enhanced (testis).
DR MalaCards; CDC14A; -.
DR MIM; 603504; gene.
DR MIM; 608653; phenotype.
DR neXtProt; NX_Q9UNH5; -.
DR OpenTargets; ENSG00000079335; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA26254; -.
DR VEuPathDB; HostDB:ENSG00000079335; -.
DR eggNOG; KOG1720; Eukaryota.
DR GeneTree; ENSGT00940000155899; -.
DR HOGENOM; CLU_017787_0_2_1; -.
DR InParanoid; Q9UNH5; -.
DR OMA; QPTARNY; -.
DR OrthoDB; 1357618at2759; -.
DR PhylomeDB; Q9UNH5; -.
DR TreeFam; TF101053; -.
DR PathwayCommons; Q9UNH5; -.
DR Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR SignaLink; Q9UNH5; -.
DR SIGNOR; Q9UNH5; -.
DR BioGRID-ORCS; 8556; 11 hits in 1086 CRISPR screens.
DR ChiTaRS; CDC14A; human.
DR GeneWiki; CDC14A; -.
DR GenomeRNAi; 8556; -.
DR Pharos; Q9UNH5; Tbio.
DR PRO; PR:Q9UNH5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UNH5; protein.
DR Bgee; ENSG00000079335; Expressed in sperm and 145 other tissues.
DR ExpressionAtlas; Q9UNH5; baseline and differential.
DR Genevisible; Q9UNH5; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:1902636; C:kinociliary basal body; ISS:UniProtKB.
DR GO; GO:0060091; C:kinocilium; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0032426; C:stereocilium tip; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0007096; P:regulation of exit from mitosis; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR044506; CDC14_C.
DR InterPro; IPR029260; DSPn.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR026068; Dual_Pase_CDC14A.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23339:SF77; PTHR23339:SF77; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell projection;
KW Cytoplasm; Cytoskeleton; Deafness; Disease variant; Hearing; Hydrolase;
KW Non-syndromic deafness; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..594
FT /note="Dual specificity protein phosphatase CDC14A"
FT /id="PRO_0000094876"
FT DOMAIN 179..336
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 7..162
FT /note="A"
FT REGION 163..176
FT /note="Linker"
FT REGION 177..343
FT /note="B"
FT REGION 396..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 174..191
FT /note="RVENGDFNWIVPGKFLAF -> VILFTPLKPTFLISKSIM (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012322"
FT VAR_SEQ 192..594
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012323"
FT VAR_SEQ 380..383
FT /note="DNLE -> VSFP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_012035"
FT VAR_SEQ 384..594
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_012036"
FT VAR_SEQ 586..594
FT /note="SLQSEYVHY -> VSAQTPPPGPQNPECNFCALPSQPRLPPKKFNSAKEAF
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_012037"
FT VAR_SEQ 586..594
FT /note="SLQSEYVHY -> CSCLLLVFRKPFLGSPLLSLPISHL (in isoform
FT 5)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047597"
FT VARIANT 139..594
FT /note="Missing (in DFNB32)"
FT /evidence="ECO:0000269|PubMed:29293958"
FT /id="VAR_081127"
FT VARIANT 312
FT /note="R -> G (in DFNB32; dbSNP:rs148737918)"
FT /evidence="ECO:0000269|PubMed:29293958"
FT /id="VAR_081128"
FT VARIANT 312
FT /note="R -> Q (in DFNB32; dbSNP:rs369245990)"
FT /evidence="ECO:0000269|PubMed:29293958"
FT /id="VAR_081129"
FT VARIANT 320
FT /note="Q -> P (in DFNB32; dbSNP:rs1339709390)"
FT /evidence="ECO:0000269|PubMed:29293958"
FT /id="VAR_081130"
FT VARIANT 339..594
FT /note="Missing (in DFNB32)"
FT /evidence="ECO:0000269|PubMed:27259055"
FT /id="VAR_081131"
FT VARIANT 345..594
FT /note="Missing (in DFNB32)"
FT /evidence="ECO:0000269|PubMed:29293958"
FT /id="VAR_081132"
FT VARIANT 345
FT /note="R -> Q (in dbSNP:rs28364897)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019957"
FT VARIANT 376..594
FT /note="Missing (in DFNB32)"
FT /evidence="ECO:0000269|PubMed:27259055,
FT ECO:0000269|PubMed:29293958"
FT /id="VAR_081133"
FT VARIANT 493
FT /note="D -> Y (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035655"
FT VARIANT 589
FT /note="S -> F (in dbSNP:rs28364923)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019958"
FT MUTAGEN 251
FT /note="D->A: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:12134069"
FT MUTAGEN 278
FT /note="C->S: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:11598127,
FT ECO:0000269|PubMed:12134069"
FT MUTAGEN 284
FT /note="R->A: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:12134069"
FT MUTAGEN 362
FT /note="M->A: Inappropriate nucleolar localization; when
FT associated with A-364."
FT /evidence="ECO:0000269|PubMed:11901424"
FT MUTAGEN 364
FT /note="I->A: Inappropriate nucleolar localization; when
FT associated with A-362."
FT /evidence="ECO:0000269|PubMed:11901424"
FT CONFLICT 164
FT /note="F -> I (in Ref. 1; AAB88277)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="W -> C (in Ref. 1; AAB88277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 66574 MW; D5552E2BAEEA84DF CRC64;
MAAESGELIG ACEFMKDRLY FATLRNRPKS TVNTHYFSID EELVYENFYA DFGPLNLAMV
YRYCCKLNKK LKSYSLSRKK IVHYTCFDQR KRANAAFLIG AYAVIYLKKT PEEAYRALLS
GSNPPYLPFR DASFGNCTYN LTILDCLQGI RKGLQHGFFD FETFDVDEYE HYERVENGDF
NWIVPGKFLA FSGPHPKSKI ENGYPLHAPE AYFPYFKKHN VTAVVRLNKK IYEAKRFTDA
GFEHYDLFFI DGSTPSDNIV RRFLNICENT EGAIAVHCKA GLGRTGTLIA CYVMKHYRFT
HAEIIAWIRI CRPGSIIGPQ QHFLEEKQAS LWVQGDIFRS KLKNRPSSEG SINKILSGLD
DMSIGGNLSK TQNMERFGED NLEDDDVEMK NGITQGDKLR ALKSQRQPRT SPSCAFRSDD
TKGHPRAVSQ PFRLSSSLQG SAVTLKTSKM ALSPSATAKR INRTSLSSGA TVRSFSINSR
LASSLGNLNA ATDDPENKKT SSSSKAGFTA SPFTNLLNGS SQPTTRNYPE LNNNQYNRSS
NSNGGNLNSP PGPHSAKTEE HTTILRPSYT GLSSSSARFL SRSIPSLQSE YVHY
